Tyrosinase biological activity

Khan MTH (2007) Recent Advances on the Sugar-Derived Heterocycles and Their Precursors as Inhibitors Against Glycogen Phosphorylases (GP). 9 33-52 Khan MTH (2007) Heterocyclic Compounds Against the Enzyme Tyrosinase Essential for Melanin Production Biochemical Features of Inhibition. 9 119-138 Khan MTH (2007) Molecular Modeling of the Biologically Active Alkaloids. 10 75-98 Khan MTH, Ather A (2007) Microbial Transformation of Nitrogenous Compoimds. 10 99-122... [Pg.311]

The group of van Maarseveen investigated the conformational properties of several amide bonds in the cyclopeptide cyclo[ProTyrProVal], which is a potent tyrosinase inhibitor, and replaced amide bonds with 1,4-substituted triazoles by CuAAC. Peptides 77 and 79 were synthesized in solution and cyclized under forcing conditions to provide the cyclo-triazolylpeptides (78 and 80 in Scheme 10.23) and both compounds retained the biological activity found in the parent cyclopeptide. [Pg.303]

The goal of our research on the multicopper oxidases has been to determine the spectral features of the type 3 (and type 2) centers, to use these spectral features to define geometric and electronic structural differences relative to hemocyanin and tyrosinase, and to understand how these structural differences contribute to their variation in biological function. The hemocyanins and tyrosinases reversibly bind and activate dioxygen whereas the multicopper oxidases catalyze its four-electron reduction to water. [Pg.158]

Copper Hemocyanrn/Tyrosinase Models Copper Proteins with Dinuclear Active Sites Copper Proteins with Type 1 Sites Copper Proteins with Type 2 Sites Cytochrome Oxidase Electron Transfer Reactions Theory Long-range Electron Transfer in Biology Metal Ion Toxicity Metal-related Diseases of Genetic Origin Metallochaperones Metal Ion Homeostasis Nutritional Aspects of Metals Trace Elements. [Pg.1013]